Structural and biological characterization of Nattectin, a new C-type lectin from the venomous fish Thalassophryne nattereri

被引:56
作者
Lopes-Ferreira, Monica [1 ]
Magalhaes, Geraldo Santana [2 ]
Fernandez, Jorge Hernandez [3 ]
Junqueira-de-Azevedo, Inacio de Loiola M. [4 ]
Le Ho, Paulo [4 ]
Lima, Carla [1 ]
Valente, Richard H. [5 ]
Moura-da-Silva, Ana Maria [2 ]
机构
[1] Inst Butantan, Lab Especial Toxinol Aplicada CEPID FAPESP, Sao Paulo, Brazil
[2] Inst Butantan, Lab Imunopatol, Sao Paulo, Brazil
[3] Univ Estadual N Fluminense Darcy Ribeiro, Lab Natl Comput Cient, Campo Goytac, Brazil
[4] Inst Butantan, Ctr Biotechnol, Sao Paulo, Brazil
[5] Inst Oswaldo Cruz Fiocruz, Lab Toxinol, Rio De Janeiro, Brazil
基金
巴西圣保罗研究基金会;
关键词
Nattectin; C-type lectin; Galactose; Inflammation; Fish venom; Thalassophryne nattereri; STONEFISH SYNANCEJA-HORRIDA; CONGER-MYRIASTER BREVOORT; CDNA CLONING; KININOGENASE ACTIVITY; ANTIFREEZE PROTEIN; INNATE IMMUNITY; BINDING; RECOGNITION; GALECTIN-3; INTEGRIN;
D O I
10.1016/j.biochi.2011.03.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Lectins are glycan-binding receptors that recognize glycan epitopes on foreign pathogens and in the host systems. They can be involved in functions that include innate immunity, development, immune regulation and homeostasis. Several lectins have been purified and characterized from fish species. In this work, using cation-exchange chromatography, a galactose-specific lectin belonging to the family of C-type lectins was isolated from the venom of the Brazilian venomous fish Thalassophryne nattereri. Nattectin is a basic, non-glycosilated, 15 kDa monomeric protein. It exhibits hemagglutination activity that is independent of Ca(2+). We also demonstrated a lectin activity for Nattectin in the innate immune system, especially in neutrophil mobilization in mice, indicating that marine organisms are source of immunomodulator agents. (C) 2011 Elsevier Masson SAS. All rights reserved.
引用
收藏
页码:971 / 980
页数:10
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